Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Carboxypeptidase N subunit 2

Gene

Cpn2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

The 83 kDa subunit binds and stabilizes the catalytic subunit at 37 degrees Celsius and keeps it in circulation. Under some circumstances it may be an allosteric modifier of the catalytic subunit (By similarity).By similarity

Names & Taxonomyi

Protein namesi
Recommended name:
Carboxypeptidase N subunit 2
Alternative name(s):
Carboxypeptidase N 83 kDa chain
Carboxypeptidase N large subunit
Carboxypeptidase N polypeptide 2
Carboxypeptidase N regulatory subunit
Gene namesi
Name:Cpn2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 16

Organism-specific databases

MGIiMGI:1919006. Cpn2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence analysisAdd
BLAST
Chaini22 – 547526Carboxypeptidase N subunit 2PRO_0000020990Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi74 – 741N-linked (GlcNAc...)2 Publications
Glycosylationi111 – 1111N-linked (GlcNAc...)1 Publication
Glycosylationi119 – 1191N-linked (GlcNAc...)1 Publication
Glycosylationi266 – 2661N-linked (GlcNAc...)Sequence analysis
Glycosylationi311 – 3111N-linked (GlcNAc...)Sequence analysis
Glycosylationi348 – 3481N-linked (GlcNAc...)1 Publication
Glycosylationi359 – 3591N-linked (GlcNAc...)1 Publication
Glycosylationi367 – 3671N-linked (GlcNAc...)1 Publication
Glycosylationi520 – 5201N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

EPDiQ9DBB9.
MaxQBiQ9DBB9.
PaxDbiQ9DBB9.
PRIDEiQ9DBB9.

Expressioni

Gene expression databases

BgeeiQ9DBB9.
CleanExiMM_CPN2.
GenevisibleiQ9DBB9. MM.

Interactioni

Subunit structurei

Tetramer of two catalytic chains and two glycosylated inactive chains.By similarity

Protein-protein interaction databases

IntActiQ9DBB9. 1 interaction.
MINTiMINT-4090020.
STRINGi10090.ENSMUSP00000069318.

Structurei

3D structure databases

ProteinModelPortaliQ9DBB9.
SMRiQ9DBB9. Positions 22-491.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini22 – 4928LRRNTAdd
BLAST
Repeati98 – 11922LRR 1Add
BLAST
Repeati122 – 14322LRR 2Add
BLAST
Repeati146 – 16722LRR 3Add
BLAST
Repeati170 – 19122LRR 4Add
BLAST
Repeati194 – 21522LRR 5Add
BLAST
Repeati218 – 23922LRR 6Add
BLAST
Repeati242 – 26322LRR 7Add
BLAST
Repeati266 – 28722LRR 8Add
BLAST
Repeati290 – 31122LRR 9Add
BLAST
Repeati314 – 33522LRR 10Add
BLAST
Repeati338 – 35922LRR 11Add
BLAST
Repeati362 – 38322LRR 12Add
BLAST
Domaini395 – 44753LRRCTAdd
BLAST

Sequence similaritiesi

Contains 12 LRR (leucine-rich) repeats.Curated
Contains 1 LRRCT domain.Curated
Contains 1 LRRNT domain.Curated

Keywords - Domaini

Leucine-rich repeat, Repeat, Signal

Phylogenomic databases

eggNOGiKOG0619. Eukaryota.
COG4886. LUCA.
GeneTreeiENSGT00760000118777.
HOGENOMiHOG000294123.
HOVERGENiHBG050814.
InParanoidiQ9DBB9.
KOiK13023.
OMAiWQCDCHL.
OrthoDBiEOG712TVW.
PhylomeDBiQ9DBB9.
TreeFamiTF351124.

Family and domain databases

Gene3Di3.80.10.10. 3 hits.
InterProiIPR000483. Cys-rich_flank_reg_C.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000372. LRRNT.
[Graphical view]
PfamiPF13855. LRR_8. 4 hits.
[Graphical view]
SMARTiSM00369. LRR_TYP. 12 hits.
SM00082. LRRCT. 1 hit.
SM00013. LRRNT. 1 hit.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 1 hit.
PROSITEiPS51450. LRR. 11 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9DBB9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFPGAWLCWV SLLLLARLTQ PCPVGCDCFG REVFCSDEQL ADIPPDIPPH
60 70 80 90 100
ITDIVFVETA FTTVRTRAFS GSPNLTKVVF LNTQVRHLEP DAFGGLPRLQ
110 120 130 140 150
DLEITGSPVS NLSAHIFSNL SSLEKLTLDF DRLAGLPEDL FCHMDILESL
160 170 180 190 200
QLQGNQLRTL PGRLFQSLRD LRTLNLAQNL LTQLPKGAFQ SLTGLQMLKL
210 220 230 240 250
SNNMLARLPE GALGSLSSLQ ELFLDGNAIT ELSPHLFSQL FSLEMLWLQH
260 270 280 290 300
NAICHLPVSL FSSLHNLTFL SLKDNALRTL PEGLFAHNQG LLHLSLSYNQ
310 320 330 340 350
LETIPEGAFT NLSRLVSLTL SHNAITDLPE HVFRNLEQLV KLSLDSNNLT
360 370 380 390 400
ALHPALFHNL SRLQLLNLSR NQLTTLPGGI FDTNYDLFNL ALLGNPWQCD
410 420 430 440 450
CHLSYLTSWL RLYNNQISNT HTFCAGPAYL KGQLVPNLKQ EQLICPVNPG
460 470 480 490 500
HLSFRALGLD EGEPAGSWDL TVEGRAAHSQ CAYSNPEGTV LLACEESRCR
510 520 530 540
WLNIQLSSRD GSDSAAMVYN SSQEWGLRSS CGLLRVTVSI EAPAAGP
Length:547
Mass (Da):60,479
Last modified:September 27, 2004 - v2
Checksum:i89437E8F32DA1453
GO

Sequence cautioni

The sequence AAH25836.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAB23775.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK005049 mRNA. Translation: BAB23775.1. Different initiation.
BC025836 mRNA. Translation: AAH25836.1. Different initiation.
BC138287 mRNA. Translation: AAI38288.1.
BC138288 mRNA. Translation: AAI38289.1.
CCDSiCCDS49819.1.
RefSeqiNP_082180.2. NM_027904.3.
XP_006522648.1. XM_006522585.1.
UniGeneiMm.290614.

Genome annotation databases

EnsembliENSMUST00000064856; ENSMUSP00000069318; ENSMUSG00000023176.
GeneIDi71756.
KEGGimmu:71756.
UCSCiuc007ywm.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK005049 mRNA. Translation: BAB23775.1. Different initiation.
BC025836 mRNA. Translation: AAH25836.1. Different initiation.
BC138287 mRNA. Translation: AAI38288.1.
BC138288 mRNA. Translation: AAI38289.1.
CCDSiCCDS49819.1.
RefSeqiNP_082180.2. NM_027904.3.
XP_006522648.1. XM_006522585.1.
UniGeneiMm.290614.

3D structure databases

ProteinModelPortaliQ9DBB9.
SMRiQ9DBB9. Positions 22-491.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9DBB9. 1 interaction.
MINTiMINT-4090020.
STRINGi10090.ENSMUSP00000069318.

Proteomic databases

EPDiQ9DBB9.
MaxQBiQ9DBB9.
PaxDbiQ9DBB9.
PRIDEiQ9DBB9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000064856; ENSMUSP00000069318; ENSMUSG00000023176.
GeneIDi71756.
KEGGimmu:71756.
UCSCiuc007ywm.1. mouse.

Organism-specific databases

CTDi1370.
MGIiMGI:1919006. Cpn2.

Phylogenomic databases

eggNOGiKOG0619. Eukaryota.
COG4886. LUCA.
GeneTreeiENSGT00760000118777.
HOGENOMiHOG000294123.
HOVERGENiHBG050814.
InParanoidiQ9DBB9.
KOiK13023.
OMAiWQCDCHL.
OrthoDBiEOG712TVW.
PhylomeDBiQ9DBB9.
TreeFamiTF351124.

Miscellaneous databases

PROiQ9DBB9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9DBB9.
CleanExiMM_CPN2.
GenevisibleiQ9DBB9. MM.

Family and domain databases

Gene3Di3.80.10.10. 3 hits.
InterProiIPR000483. Cys-rich_flank_reg_C.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000372. LRRNT.
[Graphical view]
PfamiPF13855. LRR_8. 4 hits.
[Graphical view]
SMARTiSM00369. LRR_TYP. 12 hits.
SM00082. LRRCT. 1 hit.
SM00013. LRRNT. 1 hit.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 1 hit.
PROSITEiPS51450. LRR. 11 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Liver.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Brain and Liver.
  3. "Proteome-wide characterization of N-glycosylation events by diagonal chromatography."
    Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.
    J. Proteome Res. 5:2438-2447(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-74; ASN-111; ASN-119; ASN-348; ASN-359 AND ASN-367.
    Strain: C57BL/6J.
    Tissue: Plasma.
  4. "Enhanced analysis of the mouse plasma proteome using cysteine-containing tryptic glycopeptides."
    Bernhard O.K., Kapp E.A., Simpson R.J.
    J. Proteome Res. 6:987-995(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-74.
    Strain: C57BL/6J.
    Tissue: Plasma.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen and Testis.

Entry informationi

Entry nameiCPN2_MOUSE
AccessioniPrimary (citable) accession number: Q9DBB9
Secondary accession number(s): B2RR89, Q8R113
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: September 27, 2004
Last modified: June 8, 2016
This is version 122 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.